ID A0A0D1YV55_9EURO Unreviewed; 1765 AA.
AC A0A0D1YV55;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Histone demethylase JARID1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_02063 {ECO:0000313|EMBL:KIV86452.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV86452.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV86452.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV86452.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR EMBL; KN846951; KIV86452.1; -; Genomic_DNA.
DR STRING; 1016849.A0A0D1YV55; -.
DR HOGENOM; CLU_000991_0_0_1; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15518; PHD_Ecm5p_Lid2p_like; 1.
DR CDD; cd15543; PHD_RSF1; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 75..116
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 140..233
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 466..516
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 608..774
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1669..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1765 AA; 197802 MW; B036CB25157C0A3A CRC64;
MVVPPSTGGV APATATAKAP SATRMNGAGP SMATPAFPYS ARHAPPLEMR SVERKGDPAS
RDPPSRARPY GLLEAPTYRP TEAEFRDPME YIRSISEKAS KFGICKIIPP DNWNPDFAID
TERFHFRTRR QEINLVEGGN RTNLNYLDQL AKFHKQYGAH LNRFPSVDKR PLDLYKLKKA
VEVRGGFERV CKDKKWAEIG RDLGYSGKIM SSLSTSLKNS YQRWLHPYEE WLKYAKPGVQ
EQLQNDQGGS FSPAVAPHPS PMNYPPPPPQ SAPPALGNGE PSFQPVMPPN GPVHAPPAPA
QQPGLMPAVT PISQPPIAPV PQPRPVSSSG FTAVNSGFAA VNNPGGFTAV NTLPPPIVKS
EPNGVPPPLS NQASSFLPVN PPTVTTFHSA GSPAPNGPSN PLKRTMSHDS LGDSGSEGLQ
GDDGPNGRRS KRPKKDGLPT IPGNHVPAMR SATPQVRSKS TPHRQGDKCE KCGQSDNKDS
ILACDSCDLG YHMACVDPPL TQFPEHDWHC SKCLVGTNDY GFEEGSVYSL KQFQEKAHNF
KEHYFGARMP FDPVTNTQRR PTEDDVEREF WRLVEDITES VEVEYGADIH STTHGSGFPT
VEKQPLNPYS KDPWNLNVMP FLEDSLFRHI KGDISGMTVP WLYVGMCFST FCWHNEDHYA
YSANFQHFGA TKTWYGIPGS HALRFEDAMR KAVPELFESQ PDLLFQLVTI LPPNQLRKAG
VDVYACDQRA GQFIITFPQA YHAGFNHGFN FNEAVNFAPA DWEPFGETGV QRLQEFRRQP
CFSHDELLFT AALADTTIKT AKWLAPALER TRDRELSDRA NFIHNHKAPR PHDDCSFDTL
PEVPSEACGL KVKIENGDLE EDEYQCCYCK AFSYLSQFRC HQSGKVSCLL HPLKADCCSA
TEMEKMQGLN HSLVLRYTNQ DLQNVVQKVV DKANVPEAWE AKLEALLMED ARPALRAMHT
LLSEGEKIPY PLQGLDDLAD FVKRCDEWVD EANLYLTRKQ QNRRKSEKTW RRSSLRTGKA
DDKDSEPQLT LERMKELIDD GELLGFSAAQ LENLQEKVTL IDDWRANVKR ILSGVNQAGL
EELETLLEEG RGFMAAMPEL TSLEKIFART QWLEEARQVQ KDVHSKTLDE CRDLLKRITD
LDILPQVPEA VHLSEVVRQG DFWEIKAKEL MAAEDVHYPQ LESLHGQVLQ QQFPVNKETL
EQMDVILAKN REAKRQIITL VERSHDQDFR KRPMYAHVRD VVKGFEDLNG KPHGAADLEK
ELRRHEDWMR KGKKLFGKAN APLHILEQHM KFVEEKNSFC FDLNDTFRPP VEPASREATP
AEGHEKGHLG EDEKPVFCIC RQPEAGLMIE CEICHDWYHA KCLKLARGKV KECETFTCPI
CDWRVKIPRD AARPKLEDLQ SWQDEIPDLP FQAEEEELLR RIVDKAQGFR DFVAQYTNGN
QLCRTIEEMP EMLFYLRKIE GAEVLLAYET NVFRQELHKW QPIAPEPPPI LNQSMSTRKP
RPTKQQKLMK EFGVEKPEDL PSHLRTKTYV RRKTQESFAT GPLLPKPLTE SPSAPGSTAS
PGQSHSAGNP NTPGTTRVQD STGASGPSGT IEPGVIAGSA AFDRSFAASR DPSFPNSPSS
LFSPAREQHP EVIRDAVMPT FPAESSADTR SHDPYPLFRD DAAIDGEDDL RNGLVNASPH
ETNSVRGGSP LRGEYDHIFM DMTPHDAEAS NDAVPSLEHE MSHASEALDM IRTASNDSAN
DNAELEDGDN VSKHFDEFLT GDGQN
//
